HSPB2, also known as MKBP is the most divergent member of the sHSP family with only 30% sequence identity to all other mammalian sHSPS (1). MKBP is known to associate specifically with myotonic dystrophy protein kinase (DMPK) in skeletal muscle. MKBP enhances the kinase activity of DMPK and protects it from heat-induced activation. MKBP also shows a unique nature compared to other sHSPs, in that the expression of MKBP is not induced by heat shock (2). In unstressed skeletal muscle, MKBP forms large oligomeric complexes with HSPB3 in the cytosol which are localized on mitochondria and the neuromuscular junction (1, 3). During stress, these complexes dissolve and MKBP's localization to mitochondria increases, leading to increased cell survival. Pinz et al. tried to find a distinct role for MKBP in terms of cardiac mechanics and finds that it is required for normal systolic performance and normal cardiac energetic (1). HSPB2 has also been found to be expressed in several cancer cell lines, including human breast cancer, suggesting that MKBP may be an important factor in tumor transformation and metastasis (4).

Product Type:

Antibodies

Format:

PBS, 50% glycerol, 0.02% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms | Rt

Immunogen:

Synthetic peptide

Applications:

WB | ICC/IF

Application Details:

WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

HSPB2, also known as MKBP is the most divergent member of the sHSP family with only 30% sequence identity to all other mammalian sHSPS (1). MKBP is known to associate specifically with myotonic dystrophy protein kinase (DMPK) in skeletal muscle. MKBP enhances the kinase activity of DMPK and protects it from heat-induced activation. MKBP also shows a unique nature compared to other sHSPs, in that the expression of MKBP is not induced by heat shock (2). In unstressed skeletal muscle, MKBP forms large oligomeric complexes with HSPB3 in the cytosol which are localized on mitochondria and the neuromuscular junction (1, 3). During stress, these complexes dissolve and MKBP's localization to mitochondria increases, leading to increased cell survival. Pinz et al. tried to find a distinct role for MKBP in terms of cardiac mechanics and finds that it is required for normal systolic performance and normal cardiac energetic (1). HSPB2 has also been found to be expressed in several cancer cell lines, including human breast cancer, suggesting that MKBP may be an important factor in tumor transformation and metastasis (4).

Product Type:

Antibodies

Format:

PBS, 50% glycerol, 0.02% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms | Rt

Immunogen:

Synthetic peptide

Applications:

WB | ICC/IF

Application Details:

WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Beclin 2 is a novel coiled-coil protein related to the autophagic Beclin 1 protein. It is thought to interact with Bcl-2, an anti-apoptotic protein, and is believed to function in autophagy. It has alson been found to mediate G protein-coupled receptro (GPCR) degradation (1).

Product Type:

Antibodies

Format:

PBS, 50% glycerol, 0.09% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Rt

Immunogen:

Synthetic peptide from the mid-protein of human Beclin 2

Applications:

WB | ICC/IF

Application Details:

WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Beclin 2 is a novel coiled-coil protein related to the autophagic Beclin 1 protein. It is thought to interact with Bcl-2, an anti-apoptotic protein, and is believed to function in autophagy. It has alson been found to mediate G protein-coupled receptro (GPCR) degradation (1).

Product Type:

Antibodies

Format:

PBS, 50% glycerol, 0.09% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Rt

Immunogen:

Synthetic peptide from the C-terminal of Human Beclin 2 (aa. 338-349)

Applications:

WB | ICC/IF

Application Details:

WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Beclin 2 is a novel coiled-coil protein related to the autophagic Beclin 1 protein. It is thought to interact with Bcl-2, an anti-apoptotic protein, and is believed to function in autophagy. It has alson been found to mediate G protein-coupled receptro (GPCR) degradation (1).

Product Type:

Antibodies

Format:

PBS, 50% glycerol, 0.09% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu | Ms

Immunogen:

Synthetic peptide from the C-terminal of Mouse Beclin 2 (aa. 410-421)

Applications:

WB | ICC/IF

Application Details:

WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

RAGE, the receptor for advanced glycation endproducts, is a 35 kDa transmembrane receptor of the immunoglobulin super family which was first characterized in 1992 by Neeper et al. It is also called "AGER". The increased expression of RAGE is associated with many disorders, such as diabetic vasculopathy, neuropathy, retinopathy and neuropathy, Alzheimer's disease and immune/inflammatory reactions of the vessel walls. It is reported that RAGE along with Amphoterin stimulates myoblast differentiation by the combined effect of stimulation of differentiation and inhibition of proliferation, and deregulation of RAGE expression in myoblasts might contribute to their neoplastic transformation.

Product Type:

Antibodies

Format:

PBS pH 7.4, 50% glycerol, 150mM NaCl, 0.02% sodium azide

Storage Temp:

-20ºC

Host Animal:

Rabbit

Species Reactivity:

Hu

Immunogen:

A synthesized peptide derived from human RAGE

Applications:

WB | IHC | ICC/IF

Antibody Isotype:

IgG

Application Details:

WB (1:1000), IHC (1:200); optimal dilutions for assays should be determined by the user.

Autophagy is a process of bulk protein degradation in which cytoplasmic components, including organelles, are enclosed in double-membrane structures called autophagosomes and delivered to lysosomes or vacuoles for degradation. ATG12 is the human homolog of a yeast protein involved in autophagy. ATG12 is conjugated to ATG5. The ATG12-ATG5 conjugate has an apparent molecular mass of 65 kDa. The C-terminal glycine of ATG12 is conjugated to a central lysine (lys130) of ATG5. Studies showed that over expression of ATG3 facilitated formation of the ATG12-ATG5 conjugate, suggesting that ATG3 cross-talks with the ATG12 conjugation system. ATG12 is ubiquitously expressed.

Product Type:

Antibody

Antibody Type:

Monoclonal

Format:

Lyophilized from PBS pH 7.2

Storage Temp:

After reconstitution keep aliquots at -20 °C for higher stability or at 4 °C with an appropriate antibacterial agent. Glycerol (1:1) may be added for additional stability. Avoid repetitive freeze/thaw cycles.

The Receptor for Advanced Glycation Endproducts (RAGE) is also known as the Advanced glycosylation end product-specific receptor (AGER). RAGE is expressed in endothelial cells and interacts with many molecules including advanced glycosylation end products (AGE) and amyloid beta peptide. At least 2 RAGE isoforms are produced by alternative splicing. Isoform 1 is a single-pass type I membrane protein whereas isoform 2 is secreted.

Immunohistochemistry (IHC) and Western Blotting (WB). A concentration of 1.0ug/ml is recommended for WB. Human RAGE (isoform 1) has a predicted length of 404 residues and MW of 43 kDa. A concentration of 1.0 ug/ml is recommended to detect the protein in formalin fixed and paraffin embedded tissues. Heat mediated antigen retrieval is recommended. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.

Alternative Names:

AGER; RAGE;

Accession Number:

Q15109 RAGE_HUMAN

Reconstitution:

Reconstitute in 100 ul of sterile distilled water to achieve an antibody concentration of 1 mg/ml. Centrifuge to remove any insoluble material.

Shelf Life:

12 months after purchase

Specificity:

The specificity of this antibody has been confirmed by WB and IHC against the antigen. | Human (WB, IHC), Rat (IHC). Predicted to react with mouse due to sequence homology

Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.

Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits ZCCHC11/TUT4 uridylyltransferase. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity).

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